Combinatorial reshaping of the Candida antarctica lipase A substrate pocket for enantioselectivity using an extremely condensed library

Proceedings of the National Academy of Sciences of the United States of America

Volumn 109, Issue 1, 2012, Pages 78-83

  Sandström, Anders G ^a   Wikmark, Ylva ^a   Engström, Karin ^a   Nyhlén, Jonas ^a   Bäckvall, Jan E ^a  

^a STOCKHOLM UNIVERSITY   (Sweden)

Author keywords

Enzyme catalysis; Kinetic resolution; Library design; Protein design

Indexed keywords

ACID LIPASE; CYSTEINE; GLYCINE; HYDROLASE; PHENYLALANINE; VALINE;

ARTICLE; CANDIDA ANTARCTICA; ENANTIOSELECTIVITY; ENZYME ACTIVE SITE; HYDROLYSIS; MOLECULAR DYNAMICS; NONHUMAN; PEPTIDE LIBRARY; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN ENGINEERING; PROTEIN FUNCTION; SITE DIRECTED MUTAGENESIS; SUBSTITUTION REACTION; WILD TYPE;

AMINO ACID SUBSTITUTION; CANDIDA; CATALYTIC DOMAIN; ESTERS; HOMOLOGOUS RECOMBINATION; IBUPROFEN; LIPASE; MODELS, MOLECULAR; MUTAGENESIS; MUTANT PROTEINS; MUTATION; PEPTIDE LIBRARY; PROTEIN CONFORMATION; STEREOISOMERISM; SUBSTRATE SPECIFICITY;

CANDIDA ANTARCTICA;

EID: 84856021987     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1111537108     Document Type: Article

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